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• W2052179482 abstract "H-protein of the glycine cleavage system has a lipoic acid prosthetic group. Selenolipoic acid is a lipoic acid analog in which both sulfur atoms are replaced by selenium atoms. Two isoforms of bovine lipoyltransferase that are responsible for the attachment of lipoic acid to H-protein had an affinity for selenolipoyl-AMP and transferred the selenolipoyl moiety to bovine apoH-protein comparable to lipoyl-AMP. Selenolipoylated H-protein was overexpressed inEscherichia coli and purified. Selenolipoylated H-protein was 26% as effective as lipoylated H-protein in the glycine decarboxylation reaction, in which reduction of the diselenide bond of selenolipoylated H-protein is catalyzed by P-protein. The diselenide form of selenolipoylated H-protein was a poor substrate for L-protein, and the rate of reduction was 0.5% of that of lipoylated H-protein. The rate of the overall glycine cleavage reaction with selenolipoylated H-protein was <1% of that with lipoylated H-protein. These results are consistent with the difference in the redox potential between the diselenide and disulfide bonds. In contrast, selenolipoylated H-protein showed three times as high glycine-14CO2exchange activity as lipoylated H-protein, presumably because the rate of reoxidation of reduced selenolipoylated H-protein is much higher than that of lipoylated H-protein. H-protein of the glycine cleavage system has a lipoic acid prosthetic group. Selenolipoic acid is a lipoic acid analog in which both sulfur atoms are replaced by selenium atoms. Two isoforms of bovine lipoyltransferase that are responsible for the attachment of lipoic acid to H-protein had an affinity for selenolipoyl-AMP and transferred the selenolipoyl moiety to bovine apoH-protein comparable to lipoyl-AMP. Selenolipoylated H-protein was overexpressed inEscherichia coli and purified. Selenolipoylated H-protein was 26% as effective as lipoylated H-protein in the glycine decarboxylation reaction, in which reduction of the diselenide bond of selenolipoylated H-protein is catalyzed by P-protein. The diselenide form of selenolipoylated H-protein was a poor substrate for L-protein, and the rate of reduction was 0.5% of that of lipoylated H-protein. The rate of the overall glycine cleavage reaction with selenolipoylated H-protein was <1% of that with lipoylated H-protein. These results are consistent with the difference in the redox potential between the diselenide and disulfide bonds. In contrast, selenolipoylated H-protein showed three times as high glycine-14CO2exchange activity as lipoylated H-protein, presumably because the rate of reoxidation of reduced selenolipoylated H-protein is much higher than that of lipoylated H-protein. The glycine cleavage system is a multienzyme complex that catalyzes the oxidative cleavage of glycine as presented in Equation 1(1Fujiwara K. Okamura K. Motokawa Y. Arch. Biochem. Biophys. 1979; 197: 454-462Crossref PubMed Scopus (50) Google Scholar, 2Fujiwara K. Motokawa Y. J. Biol. Chem. 1983; 258: 8156-8162Abstract Full Text PDF PubMed Google Scholar, 3Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1984; 259: 10664-10668Abstract Full Text PDF PubMed Google Scholar, 4Okamura-Ikeda K. Fujiwara K. Motokawa Y. J. Biol. Chem. 1987; 262: 6746-6749Abstract Full Text PDF PubMed Google Scholar),Glycine+H4folate+NAD+=CO2+NH3+5,10­CH2­H4folate+NADH+H+Equation 1 where H4folate is tetrahydrofolate. The system is composed of four proteins termed P-, H-, T- and L-proteins. The multienzyme complex performs the following series of reactions (Equations Equation 2, Equation 3, Equation 4),CH2(NH2)COOH+H­protein­lipS2=CO2+H­protein­lip(SH)SCH2NH2Equation 2 H­protein­lip(SH)SCH2NH2+H4folate=NH3+5,10­CH2­H4folate+H­protein­lip(SH) 2Equation 3 H­protein­lip(SH) 2+NAD+=H­protein­lipS2+NADH+H+Equation 4 where lip is lipoic acid. P-protein, which contains pyridoxal phosphate as a cofactor, catalyzes the decarboxylation of glycine and transfers the remaining aminomethyl moiety to one of the sulfhydryl groups of the lipoyl prosthetic group of H-protein (Equation 2). The aminomethyl moiety is cleaved by the action of T-protein in the presence of tetrahydrofolate, yielding ammonia and methylenetetrahydrofolate (Equation 3). The dihydrolipoyl group of H-protein is reoxidized by L-protein (Equation 4). During the catalytic cycle, the lipoyl group of H-protein functions as a carrier of the intermediate and reducing equivalents among the active sites of other component enzymes in a manner similar to that found for α-ketoacid dehydrogenase complexes (5Reed L.J. Hackert M.L. J. Biol. Chem. 1990; 265: 8971-8974Abstract Full Text PDF PubMed Google Scholar, 6Perham R.N. Biochemistry. 1991; 30: 8501-8512Crossref PubMed Scopus (362) Google Scholar).Lipoic acid attaches to the specific lysine residue of H-protein via an amide linkage. Attachment of lipoic acid to the protein involves two consecutive reactions, the activation of lipoic acid to lipoyl-AMP and the transfer of the lipoyl group to the apoprotein. In mammals, the two reactions are catalyzed by separate enzymes in mitochondria: lipoate-activating enzyme catalyzes the former reaction, and lipoyl-AMP:N ε-lysine lipoyltransferase (lipoyltransferase) catalyzes the latter (7Tsunoda J.N. Yasunobu K.T. Arch. Biochem. Biophys. 1967; 118: 395-401Crossref PubMed Scopus (27) Google Scholar, 8Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1994; 269: 16605-16609Abstract Full Text PDF PubMed Google Scholar). We have purified two isoforms of lipoyltransferase, lipoyltransferases I and II, from bovine liver. They transfer not only the lipoyl group, but also C6, C8, and C10 acyl groups from each activated adenylated form to apoH-protein and also catalyze lipoylation of lipoyl domains of the acyltransferase components of the pyruvate, α-ketoglutarate, and branched chain α-ketoacid dehydrogenase complexes (8Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1994; 269: 16605-16609Abstract Full Text PDF PubMed Google Scholar, 9Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1996; 271: 12932-12936Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar).Selenolipoic acid is a lipoic acid analog in which both of the sulfur atoms are replaced by selenium atoms. Studies with wild-typeEscherichia coli have shown that selenolipoic acid inhibits growth of the bacteria through formation of selenolipoylated α-ketoacid dehydrogenase complexes that are nonfunctional (10Reed K.E. Morris T.W. Cronan Jr., J.E. Proc. Natl. Acad. Sci. U. S. A. 1994; 91: 3720-3724Crossref PubMed Scopus (28) Google Scholar). In mammals, the biological properties of selenolipoic acid have not been elucidated so far. In this study, we show that selenolipoic acid can serve as a substrate for bovine lipoyltransferase. Additionally, we overexpressed selenolipoylated recombinant bovine H-protein in E. coli and characterized the function of selenolipoylated H-protein in the glycine cleavage reaction. The glycine cleavage system is a multienzyme complex that catalyzes the oxidative cleavage of glycine as presented in Equation 1(1Fujiwara K. Okamura K. Motokawa Y. Arch. Biochem. Biophys. 1979; 197: 454-462Crossref PubMed Scopus (50) Google Scholar, 2Fujiwara K. Motokawa Y. J. Biol. Chem. 1983; 258: 8156-8162Abstract Full Text PDF PubMed Google Scholar, 3Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1984; 259: 10664-10668Abstract Full Text PDF PubMed Google Scholar, 4Okamura-Ikeda K. Fujiwara K. Motokawa Y. J. Biol. Chem. 1987; 262: 6746-6749Abstract Full Text PDF PubMed Google Scholar),Glycine+H4folate+NAD+=CO2+NH3+5,10­CH2­H4folate+NADH+H+Equation 1 where H4folate is tetrahydrofolate. The system is composed of four proteins termed P-, H-, T- and L-proteins. The multienzyme complex performs the following series of reactions (Equations Equation 2, Equation 3, Equation 4),CH2(NH2)COOH+H­protein­lipS2=CO2+H­protein­lip(SH)SCH2NH2Equation 2 H­protein­lip(SH)SCH2NH2+H4folate=NH3+5,10­CH2­H4folate+H­protein­lip(SH) 2Equation 3 H­protein­lip(SH) 2+NAD+=H­protein­lipS2+NADH+H+Equation 4 where lip is lipoic acid. P-protein, which contains pyridoxal phosphate as a cofactor, catalyzes the decarboxylation of glycine and transfers the remaining aminomethyl moiety to one of the sulfhydryl groups of the lipoyl prosthetic group of H-protein (Equation 2). The aminomethyl moiety is cleaved by the action of T-protein in the presence of tetrahydrofolate, yielding ammonia and methylenetetrahydrofolate (Equation 3). The dihydrolipoyl group of H-protein is reoxidized by L-protein (Equation 4). During the catalytic cycle, the lipoyl group of H-protein functions as a carrier of the intermediate and reducing equivalents among the active sites of other component enzymes in a manner similar to that found for α-ketoacid dehydrogenase complexes (5Reed L.J. Hackert M.L. J. Biol. Chem. 1990; 265: 8971-8974Abstract Full Text PDF PubMed Google Scholar, 6Perham R.N. Biochemistry. 1991; 30: 8501-8512Crossref PubMed Scopus (362) Google Scholar). Lipoic acid attaches to the specific lysine residue of H-protein via an amide linkage. Attachment of lipoic acid to the protein involves two consecutive reactions, the activation of lipoic acid to lipoyl-AMP and the transfer of the lipoyl group to the apoprotein. In mammals, the two reactions are catalyzed by separate enzymes in mitochondria: lipoate-activating enzyme catalyzes the former reaction, and lipoyl-AMP:N ε-lysine lipoyltransferase (lipoyltransferase) catalyzes the latter (7Tsunoda J.N. Yasunobu K.T. Arch. Biochem. Biophys. 1967; 118: 395-401Crossref PubMed Scopus (27) Google Scholar, 8Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1994; 269: 16605-16609Abstract Full Text PDF PubMed Google Scholar). We have purified two isoforms of lipoyltransferase, lipoyltransferases I and II, from bovine liver. They transfer not only the lipoyl group, but also C6, C8, and C10 acyl groups from each activated adenylated form to apoH-protein and also catalyze lipoylation of lipoyl domains of the acyltransferase components of the pyruvate, α-ketoglutarate, and branched chain α-ketoacid dehydrogenase complexes (8Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1994; 269: 16605-16609Abstract Full Text PDF PubMed Google Scholar, 9Fujiwara K. Okamura-Ikeda K. Motokawa Y. J. Biol. Chem. 1996; 271: 12932-12936Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar). Selenolipoic acid is a lipoic acid analog in which both of the sulfur atoms are replaced by selenium atoms. Studies with wild-typeEscherichia coli have shown that selenolipoic acid inhibits growth of the bacteria through formation of selenolipoylated α-ketoacid dehydrogenase complexes that are nonfunctional (10Reed K.E. Morris T.W. Cronan Jr., J.E. Proc. Natl. Acad. Sci. U. S. A. 1994; 91: 3720-3724Crossref PubMed Scopus (28) Google Scholar). In mammals, the biological properties of selenolipoic acid have not been elucidated so far. In this study, we show that selenolipoic acid can serve as a substrate for bovine lipoyltransferase. Additionally, we overexpressed selenolipoylated recombinant bovine H-protein in E. coli and characterized the function of selenolipoylated H-protein in the glycine cleavage reaction. We thank Dr. Shiro Futaki (Faculty of Pharmaceutical Sciences, University of Tokushima) for help in the molecular mass determinations and ASTA-Medica for the generous gift of selenolipoic acid." @default.
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• W2052179482 date "1997-08-01" @default.
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• W2052179482 title "Synthesis and Characterization of Selenolipoylated H-protein of the Glycine Cleavage System" @default.
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